Evidence map›Paper›PMID 20190047›Full record

ArticleJournal of bacteriology2010

Characterization of Acp, a peptidoglycan hydrolase of Clostridium perfringens with N-acetylglucosaminidase activity that is implicated in cell separation and stress-induced autolysis.

Emilie Camiade, Johann Peltier, Ingrid Bourgeois, Evelyne Couture-Tosi, Pascal Courtin, Ana Antunes, Marie-Pierre Chapot-Chartier, Bruno Dupuy, Jean-Louis Pons

Open access · greenAbstract read
In one paragraph

Article in Journal of bacteriology, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.

0numbers the graph read from it
0cells of the map it votes in
17citing papers in PubMed
1.8field-weighted citation impact, top 15% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

17 citing papers in PubMed, 35 citations in OpenAlex.

  1. Article
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  4. Structural Investigations on the SH3b Domains ofMolecules (Basel, Switzerland) · 2021
    Article
  5. The Human Gut MicrobeAntibiotics (Basel, Switzerland) · 2021
    Article
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4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

9 authors at 3 institutions in 1 country.

Emilie CamiadeGroupe de Recherche sur les Antimicrobiens et les Micro-organismes, UPRES EA 2656, IFR 23, Université de Rouen, 22 Boulevard Gambetta, F-76183 Rouen Cedex, France.
Johann Peltier
Ingrid Bourgeois
Evelyne Couture-Tosi
Pascal Courtin
Ana Antunes
Marie-Pierre Chapot-Chartier
Bruno Dupuy
Jean-Louis Pons
Université de Rouen Normandie · FRInstitut Pasteur · FRMicrobiologie de l’alimentation au service de la santé · FR

Funding

PHS HHS A1057637
6 · The paper itself

Abstract

This work reports the characterization of the first known peptidoglycan hydrolase (Acp) produced mainly during vegetative growth of Clostridium perfringens. Acp has a modular structure with three domains: a signal peptide domain, an N-terminal domain with repeated sequences, and a C-terminal catalytic domain. The purified recombinant catalytic domain of Acp displayed lytic activity on the cell walls of several Gram-positive bacterial species. Its hydrolytic specificity was established by analyzing the Bacillus subtilis peptidoglycan digestion products by coupling reverse phase-high-pressure liquid chromatography (RP-HPLC) and matrix-assisted laser desorption ionization-time of flight mass spectrometry (MALDI-TOF MS) analysis, which displayed an N-acetylglucosaminidase activity. The study of acp expression showed a constant expression during growth, which suggested an important role of Acp in growth of C. perfringens. Furthermore, cell fractionation and indirect immunofluorescence staining using anti-Acp antibodies revealed that Acp is located at the septal peptidoglycan of vegetative cells during exponential growth phase, indicating a role in cell separation or division of C. perfringens. A knockout acp mutant strain was obtained by using the insertion of mobile group II intron strategy (ClosTron). The microscopic examination indicated a lack of vegetative cell separation in the acp mutant strain, as well as the wild-type strain incubated with anti-Acp antibodies, demonstrating the critical role of Acp in cell separation. The comparative responses of wild-type and acp mutant strains to stresses induced by Triton X-100, bile salts, and vancomycin revealed an implication of Acp in autolysis induced by these stresses. Overall, Acp appears as a major cell wall N-acetylglucosaminidase implicated in both vegetative growth and stress-induced autolysis.

Indexed as

AcetylglucosaminidaseAnti-Bacterial AgentsBacterial ProteinsBacteriolysisBlotting, WesternChromatography, High Pressure LiquidClostridium perfringensElectrophoresis, Polyacrylamide GelGenome, BacterialMicrobial Sensitivity TestsMolecular Sequence DataMutagenesisN-Acetylmuramoyl-L-alanine AmidaseOctoxynolPeptidoglycanReverse Transcriptase Polymerase Chain ReactionAcetylglucosaminidaseAnti-Bacterial AgentsBacterial ProteinsN-Acetylmuramoyl-L-alanine AmidaseOctoxynolPeptidoglycan

Identifiers

PMID20190047
PMCPMC2863477
OpenAlexW2144948701

What OpenQuestion holds

Textmetadata
Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.